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Q466X0 (AMPPA_METBF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP phosphorylase

Short name=AMPpase
EC=2.4.2.57
Alternative name(s):
Nucleoside monophosphate phosphorylase
Short name=NMP phosphorylase
Gene names
Ordered Locus Names:Mbar_A3188
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO By similarity. HAMAP-Rule MF_02132

Catalytic activity

AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate. HAMAP-Rule MF_02132

CMP + phosphate = cytosine + alpha-D-ribose 1,5-bisphosphate. HAMAP-Rule MF_02132

UMP + phosphate = uracil + alpha-D-ribose 1,5-bisphosphate. HAMAP-Rule MF_02132

Sequence similarities

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 506506AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000225645

Regions

Nucleotide binding193 – 1986AMP By similarity

Sites

Active site2551Proton donor By similarity
Binding site1671AMP; via amide nitrogen By similarity
Binding site2021AMP; via amide nitrogen By similarity
Binding site2631AMP By similarity
Binding site2871AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q466X0 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: CA65A31C8EDAE32E

FASTA50654,628
        10         20         30         40         50         60 
MQLKLEHFNI KIGQHKILLN IADAKELGVN PGDRVRIRGR ESISAIADTT DDMVPPGTLG 

        70         80         90        100        110        120 
VFSEVYEHFV NWDKPVEVVP AFRSKSASVI KKMMDKKPVV QEEIKTLVND IVEENLSEIE 

       130        140        150        160        170        180 
LSAFITSSYI HGMTDDEVEW LTRAMIESGD TIEFDTHPIM DKHSIGGVPG NKISLLVVPI 

       190        200        210        220        230        240 
IAANGLLIPK TSSRAITGAG GTADLMEVLC PVEFSSQEVK EITEKVGGAL VWGGATNIAP 

       250        260        270        280        290        300 
ADDKLIRVEY PLSIDPYYQM LASIMAKKGA IGADNVVMDI PVGPSTKVPT VQEGQKLARD 

       310        320        330        340        350        360 
LINLGHRLGM NVECAITYGS SPIGRKVGPS LEVREALKVL ESMEGPNSLI EKSAALAGIL 

       370        380        390        400        410        420 
LEMGGAAPRD RGKEIALETL RSGKALEKMK QIIEAQGGDP KITSADIQVG QYTADILASA 

       430        440        450        460        470        480 
DGYVIEFDNK WIIEIARLAG APNDKGAGVA IHKKMGESVK KGDPILTIYA EKEFKLETAL 

       490        500 
ATAQRTNPIV VEGMLLKRIP GTYGFQ 

« Hide

References

[1]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fusaro / DSM 804.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000099 Genomic DNA. Translation: AAZ72072.1.
RefSeqYP_306652.1. NC_007355.1.

3D structure databases

ProteinModelPortalQ466X0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269797.Mbar_A3188.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ72072; AAZ72072; Mbar_A3188.
GeneID3627130.
KEGGmba:Mbar_A3188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAFINGVRD.

Enzyme and pathway databases

BioCycMBAR269797:GHUW-3243-MONOMER.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPMF_02132. AMP_phosphorylase.
InterProIPR017713. AMP_phosphorylase.
IPR009010. Asp_de-COase-like_dom.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
IPR013466. Thymidine/AMP_Pase.
[Graphical view]
PANTHERPTHR10515. PTHR10515. 1 hit.
PfamPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFPIRSF000478. TP_PyNP. 1 hit.
SMARTSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMSSF47648. SSF47648. 1 hit.
SSF50692. SSF50692. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsTIGR03327. AMP_phos. 1 hit.
TIGR02645. ARCH_P_rylase. 1 hit.
PROSITEPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPPA_METBF
AccessionPrimary (citable) accession number: Q466X0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families